Chlorine in PDB 8ttj: Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan

The structure of Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan, PDB code: 8ttj was solved by K.Lingkon, J.J.Bellizzi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.47 / 1.98
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	73.52, 157.971, 112.58, 90, 104.06, 90
R / Rfree (%)	19.9 / 23.7

The binding sites of Chlorine atom in the Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan (pdb code 8ttj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan, PDB code: 8ttj:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:33.5 occ:1.00 CLL A:6CW601 0.0 33.5 1.0 CH2 A:6CW601 1.8 19.8 1.0 CZ3 A:6CW601 2.7 25.2 1.0 CZ2 A:6CW601 2.8 21.6 1.0 NZ A:LYS79 3.2 37.1 1.0 OE1 A:GLU357 3.2 26.8 1.0 O A:GLU357 3.6 31.4 1.0 CG1 A:VAL82 3.6 32.1 1.0 C A:GLU357 3.7 30.4 1.0 CE A:LYS79 3.8 31.4 1.0 OG A:SER358 3.8 34.8 1.0 CA A:GLU357 3.9 24.5 1.0 CE3 A:6CW601 4.0 25.3 1.0 CB A:VAL82 4.0 18.6 1.0 CE2 A:6CW601 4.1 22.8 1.0 CB A:SER358 4.2 36.5 1.0 CD A:GLU357 4.4 16.9 1.0 CB A:GLU357 4.4 19.2 1.0 N A:SER358 4.4 25.5 1.0 CD2 A:6CW601 4.6 20.8 1.0 CE1 A:PHE111 4.6 16.9 1.0 ND1 A:HIS109 4.7 22.7 1.0 N A:VAL82 4.8 20.3 1.0 CZ A:PHE111 4.8 19.4 1.0 CA A:SER358 4.9 29.9 1.0 O A:LEU356 5.0 21.6 1.0

Chlorine binding site 2 out of 4 in the Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl601 b:44.6 occ:1.00 CLL B:6CW601 0.0 44.6 1.0 CH2 B:6CW601 1.7 25.5 1.0 CZ3 B:6CW601 2.6 24.3 1.0 CZ2 B:6CW601 2.8 23.8 1.0 NZ B:LYS79 3.0 31.4 1.0 CG2 B:VAL82 3.1 36.0 1.0 O B:GLU357 3.2 23.8 1.0 OE1 B:GLU357 3.3 29.6 1.0 C B:GLU357 3.5 24.9 1.0 OG B:SER358 3.7 49.0 1.0 CA B:GLU357 3.8 28.1 1.0 CE B:LYS79 3.8 28.5 1.0 CB B:SER358 3.9 38.7 1.0 CE3 B:6CW601 3.9 25.8 1.0 CE2 B:6CW601 4.1 26.4 1.0 N B:SER358 4.2 29.4 1.0 CB B:GLU357 4.4 28.9 1.0 CB B:VAL82 4.4 26.9 1.0 CD2 B:6CW601 4.5 27.5 1.0 CD B:GLU357 4.5 29.7 1.0 CA B:SER358 4.6 30.8 1.0 CE1 B:PHE111 4.6 26.6 1.0 CZ B:PHE111 4.9 26.3 1.0 ND1 B:HIS109 5.0 21.0 1.0

Chlorine binding site 3 out of 4 in the Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl601 b:42.8 occ:1.00 CLL C:6CW601 0.0 42.8 1.0 CH2 C:6CW601 1.8 37.2 1.0 CZ3 C:6CW601 2.7 22.1 1.0 CZ2 C:6CW601 2.8 26.6 1.0 NZ C:LYS79 3.1 38.3 1.0 OE1 C:GLU357 3.2 26.9 1.0 O C:GLU357 3.3 39.0 1.0 OG C:SER358 3.5 40.8 1.0 CG1 C:VAL82 3.7 31.8 1.0 C C:GLU357 3.8 36.4 1.0 CE C:LYS79 3.9 37.2 1.0 CE3 C:6CW601 4.0 27.8 1.0 CA C:GLU357 4.0 34.6 1.0 CB C:VAL82 4.1 26.9 1.0 CE2 C:6CW601 4.1 31.1 1.0 CD C:GLU357 4.4 28.9 1.0 CB C:GLU357 4.4 26.5 1.0 CE1 C:PHE111 4.6 22.6 1.0 CD2 C:6CW601 4.6 33.3 1.0 CB C:SER358 4.6 46.2 1.0 N C:SER358 4.7 31.6 1.0 ND1 C:HIS109 4.7 21.4 1.0 CZ C:PHE111 4.8 24.8 1.0 N C:VAL82 4.8 24.3 1.0

Chlorine binding site 4 out of 4 in the Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Tryptophan-6-Halogenase Borh Complexed with 6-Chlorotryptophan within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl601 b:58.0 occ:1.00 CLL D:6CW601 0.0 58.0 1.0 CH2 D:6CW601 1.7 40.9 1.0 CZ3 D:6CW601 2.6 33.3 1.0 CZ2 D:6CW601 2.8 35.5 1.0 OG D:SER358 2.9 45.4 1.0 O D:GLU357 3.0 50.2 1.0 NZ D:LYS79 3.1 45.0 1.0 CG2 D:VAL82 3.2 48.6 1.0 OE1 D:GLU357 3.2 42.6 1.0 C D:GLU357 3.3 45.5 1.0 CA D:GLU357 3.6 41.3 1.0 CE3 D:6CW601 3.9 34.2 1.0 N D:SER358 4.0 34.2 1.0 CB D:SER358 4.0 53.8 1.0 CE D:LYS79 4.1 38.3 1.0 CE2 D:6CW601 4.1 40.6 1.0 CB D:GLU357 4.1 37.0 1.0 CD D:GLU357 4.3 40.7 1.0 CD2 D:6CW601 4.5 30.7 1.0 CA D:SER358 4.5 36.0 1.0 CB D:VAL82 4.6 38.0 1.0 CE1 D:PHE111 4.7 41.0 1.0 O D:SER358 4.8 40.8 1.0 CG D:GLU357 4.9 29.7 1.0 CZ D:PHE111 4.9 37.0 1.0 N D:GLU357 4.9 33.4 1.0 CG1 D:VAL52 5.0 34.7 1.0 O D:LEU356 5.0 44.4 1.0 ND1 D:HIS109 5.0 34.0 1.0

M.Ashaduzzaman, K.Lingkon, A.J.De Silva, J.J.Bellizzi. Crystallographic and Thermodynamic Evidence of Negative Cooperativity of Flavin and Tryptophan Binding in the Flavin-Dependent Halogenases Abeh and Borh Biorxiv 2023.
ISSN: ISSN 2692-8205
DOI: 10.1101/2023.08.22.554356